Development of an indirect immunofluorescence assay for PCV3 antibody detection based on capsid protein

Abstract Porcine circovirus type 3 (PCV3) is a novel porcine circovirus associated with porcine dermatitis and nephritis syndrome (PDNS), reproductive failure, and multisystemic inflammation. Capsid protein (Cap) encoded by PCV3 ORF2 gene has been identified as an immunogenic protein. Currently, the...

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Autores principales:	Lun Yao, Chang Li, Junwei Wang, Yufang Cheng, Ahmed H. Ghonaim, Qi Sun, Xuexiang Yu, Weijie Niu, Shengxian Fan, Qigai He
Formato:	article
Lenguaje:	EN
Publicado:	BMC 2021
Materias:	PCV3 Capsid protein Antibodies IFA Veterinary medicine SF600-1100 Public aspects of medicine RA1-1270
Acceso en línea:	https://doaj.org/article/cec15605aa0f4b33a1bcbf180f4d076e
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spelling	oai:doaj.org-article:cec15605aa0f4b33a1bcbf180f4d076e2021-11-14T12:06:20ZDevelopment of an indirect immunofluorescence assay for PCV3 antibody detection based on capsid protein10.1186/s44149-021-00015-72731-0442https://doaj.org/article/cec15605aa0f4b33a1bcbf180f4d076e2021-07-01T00:00:00Zhttps://doi.org/10.1186/s44149-021-00015-7https://doaj.org/toc/2731-0442Abstract Porcine circovirus type 3 (PCV3) is a novel porcine circovirus associated with porcine dermatitis and nephritis syndrome (PDNS), reproductive failure, and multisystemic inflammation. Capsid protein (Cap) encoded by PCV3 ORF2 gene has been identified as an immunogenic protein. Currently, there is no immunofluorescence assay (IFA) available for serological diagnosis. Here, the N-terminal 33 amino acids of Cap protein were predicted to serve as a PCV3 nuclear localization signal (NLS). Two types of recombinant plasmids were constructed for recombinant protein expression in Sf9 cells by using a baculovirus expression system: plasmid rvBac-Pc for full-length Cap protein expression and rvBac-Sc for Cap protein expression with a honeybee melittin signal peptide in place of the predicted NLS sequence. Expression of the nuclear localization sequences was further analyzed by IFA. Strong and specific fluorescence signals were observed in the nucleus of rvBac-Pc-transfected cells and in the cytoplasm of rvBac-Sc-transfected cells. No cross-reactivity was observed with porcine circovirus type 2, porcine pseudorabies virus, classical swine fever virus, or porcine reproductive and respiratory syndrome virus. In summary, we developed two fluorescence detection modes for Cap protein that can be used to detect PCV3 antibodies. This method is suitable for the diagnosis and epidemiological investigation of PCV3. This study provides a reliable detection method for monitoring PCV3 antibody level in pigs in the future.Lun YaoChang LiJunwei WangYufang ChengAhmed H. GhonaimQi SunXuexiang YuWeijie NiuShengxian FanQigai HeBMCarticlePCV3Capsid proteinAntibodiesIFAVeterinary medicineSF600-1100Public aspects of medicineRA1-1270ENAnimal Diseases, Vol 1, Iss 1, Pp 1-8 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	PCV3 Capsid protein Antibodies IFA Veterinary medicine SF600-1100 Public aspects of medicine RA1-1270
spellingShingle	PCV3 Capsid protein Antibodies IFA Veterinary medicine SF600-1100 Public aspects of medicine RA1-1270 Lun Yao Chang Li Junwei Wang Yufang Cheng Ahmed H. Ghonaim Qi Sun Xuexiang Yu Weijie Niu Shengxian Fan Qigai He Development of an indirect immunofluorescence assay for PCV3 antibody detection based on capsid protein
description	Abstract Porcine circovirus type 3 (PCV3) is a novel porcine circovirus associated with porcine dermatitis and nephritis syndrome (PDNS), reproductive failure, and multisystemic inflammation. Capsid protein (Cap) encoded by PCV3 ORF2 gene has been identified as an immunogenic protein. Currently, there is no immunofluorescence assay (IFA) available for serological diagnosis. Here, the N-terminal 33 amino acids of Cap protein were predicted to serve as a PCV3 nuclear localization signal (NLS). Two types of recombinant plasmids were constructed for recombinant protein expression in Sf9 cells by using a baculovirus expression system: plasmid rvBac-Pc for full-length Cap protein expression and rvBac-Sc for Cap protein expression with a honeybee melittin signal peptide in place of the predicted NLS sequence. Expression of the nuclear localization sequences was further analyzed by IFA. Strong and specific fluorescence signals were observed in the nucleus of rvBac-Pc-transfected cells and in the cytoplasm of rvBac-Sc-transfected cells. No cross-reactivity was observed with porcine circovirus type 2, porcine pseudorabies virus, classical swine fever virus, or porcine reproductive and respiratory syndrome virus. In summary, we developed two fluorescence detection modes for Cap protein that can be used to detect PCV3 antibodies. This method is suitable for the diagnosis and epidemiological investigation of PCV3. This study provides a reliable detection method for monitoring PCV3 antibody level in pigs in the future.
format	article
author	Lun Yao Chang Li Junwei Wang Yufang Cheng Ahmed H. Ghonaim Qi Sun Xuexiang Yu Weijie Niu Shengxian Fan Qigai He
author_facet	Lun Yao Chang Li Junwei Wang Yufang Cheng Ahmed H. Ghonaim Qi Sun Xuexiang Yu Weijie Niu Shengxian Fan Qigai He
author_sort	Lun Yao
title	Development of an indirect immunofluorescence assay for PCV3 antibody detection based on capsid protein
title_short	Development of an indirect immunofluorescence assay for PCV3 antibody detection based on capsid protein
title_full	Development of an indirect immunofluorescence assay for PCV3 antibody detection based on capsid protein
title_fullStr	Development of an indirect immunofluorescence assay for PCV3 antibody detection based on capsid protein
title_full_unstemmed	Development of an indirect immunofluorescence assay for PCV3 antibody detection based on capsid protein
title_sort	development of an indirect immunofluorescence assay for pcv3 antibody detection based on capsid protein
publisher	BMC
publishDate	2021
url	https://doaj.org/article/cec15605aa0f4b33a1bcbf180f4d076e
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Development of an indirect immunofluorescence assay for PCV3 antibody detection based on capsid protein

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